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首页> 外文期刊>PLoS Biology >An Endoribonuclease Functionally Linked to Perinuclear mRNP Quality Control Associates with the Nuclear Pore Complexes
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An Endoribonuclease Functionally Linked to Perinuclear mRNP Quality Control Associates with the Nuclear Pore Complexes

机译：核糖核酸内切酶在功能上与核孔复合体相关联的核内mRNP质量控制

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Nuclear mRNA export is a crucial step in eukaryotic gene expression, which is in yeast coupled to cotranscriptional messenger ribonucleoprotein particle (mRNP) assembly and surveillance. Several surveillance systems that monitor nuclear mRNP biogenesis and export have been described, but the mechanism by which the improper mRNPs are recognized and eliminated remains poorly understood. Here we report that the conserved PIN domain protein Swt1 is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). Swt1 showed endoribonuclease activity in vitro that was inhibited by a point mutation in the predicted catalytic site. Swt1 lacked clear sequence specificity but showed a strong preference for single-stranded regions. Genetic interactions were found between Swt1 and the THO/TREX and TREX-2 complexes, and with components of the perinuclear mRNP surveillance system, Mlp1, Nup60, and Esc1. Inhibition of the nuclease activity of Swt1 increased the levels and cytoplasmic leakage of unspliced aberrant pre-mRNA, and induced robust nuclear poly(A)+ RNA accumulation in mlp1Δ and esc1Δ strains. Overexpression of Swt1 also caused strong nuclear poly(A)+ RNA accumulation. Swt1 is normally distributed throughout the nucleus and cytoplasm but becomes concentrated at nuclear pore complexes (NPCs) in the nup133Δ mutant, which causes NPC clustering and defects in mRNP export. The data suggest that Swt1 endoribonuclease might be transiently recruited to NPCs to initiate the degradation of defective pre-mRNPs or mRNPs trapped at nuclear periphery in order to avoid their cytoplasmic export and translation.
机译：核mRNA的输出是真核基因表达中至关重要的一步，这是在酵母中与共转录信使核糖蛋白颗粒（mRNP）组装和监测偶联的。已经描述了几种监测核mRNP生物发生和输出的监测系统，但是人们认识并发现了不正确的mRNP清除的机制。在这里我们报告保守的PIN域蛋白Swt1是一种RNA内切酶，参与核mRNPs的质量控制，并且可以与核孔复合体（NPC）结合。 Swt1在体外显示出核糖核酸内切酶活性，该活性被预测的催化位点中的点突变抑制。 Swt1缺乏明确的序列特异性，但显示出对单链区域的强烈偏好。发现Swt1与THO / TREX和TREX-2复合物之间以及与核周mRNP监测系统的组成部分Mlp1，Nup60和Esc1之间存在遗传相互作用。抑制Swt1的核酸酶活性增加了未剪接的异常pre-mRNA的水平和细胞质泄漏，并在mlp1Δ和esc1Δ菌株中诱导了健壮的核poly（A）+ RNA积累。 Swt1的过表达还引起强烈的核poly（A）+ RNA积累。 Swt1通常分布在整个细胞核和细胞质中，但集中在nup133Δ突变体的核孔复合体（NPC）上，这会导致NPC聚集和mRNP出口缺陷。数据表明，Swt1内切核糖核酸酶可能会被短暂地招募到NPC，以启动有缺陷的前mRNPs或困在核外围的mRNPs的降解，以避免它们的胞质输出和翻译。

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